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Protein

Protein FimF

Gene

fimF

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Involved in regulation of length and mediation of adhesion of type 1 fimbriae (but not necessary for the production of fimbriae). Involved in the integration of FimH in the fimbriae.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei175 – 1751Required for stability and transportBy similarity

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

BioCyciEcoCyc:EG10313-MONOMER.
ECOL316407:JW4281-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein FimF
Gene namesi
Name:fimF
Ordered Locus Names:b4318, JW4281
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10313. fimF.

Subcellular locationi

GO - Cellular componenti

  • pilus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Fimbrium

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence analysisAdd
BLAST
Chaini21 – 176156Protein FimFPRO_0000009207Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi38 ↔ 78Curated

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP08189.

Interactioni

Protein-protein interaction databases

BioGridi4262749. 3 interactions.
DIPiDIP-9614N.
IntActiP08189. 1 interaction.
MINTiMINT-6491069.
STRINGi511145.b4318.

Structurei

Secondary structure

1
176
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi25 – 3410Combined sources
Beta strandi35 – 373Combined sources
Beta strandi38 – 425Combined sources
Beta strandi46 – 494Combined sources
Helixi52 – 554Combined sources
Helixi56 – 583Combined sources
Beta strandi69 – 7810Combined sources
Beta strandi84 – 907Combined sources
Beta strandi100 – 1023Combined sources
Beta strandi106 – 1094Combined sources
Beta strandi111 – 1188Combined sources
Beta strandi127 – 1293Combined sources
Helixi131 – 1333Combined sources
Beta strandi136 – 1383Combined sources
Beta strandi141 – 1433Combined sources
Beta strandi145 – 15915Combined sources
Beta strandi166 – 17510Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JMRNMR-A23-176[»]
3BFQX-ray1.34F23-37[»]
3BFWX-ray1.80B/D23-37[»]
3BWUX-ray1.76F35-176[»]
3JWNX-ray2.69E/F/K/L23-176[»]
4J3OX-ray3.80F23-176[»]
4XOBX-ray3.00B/D/F/H23-37[»]
ProteinModelPortaliP08189.
SMRiP08189. Positions 23-176.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08189.

Family & Domainsi

Sequence similaritiesi

Belongs to the fimbrial protein family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4108SQA. Bacteria.
ENOG4111HFM. LUCA.
HOGENOMiHOG000260127.
InParanoidiP08189.
KOiK07348.
OMAiYVRDNAC.
OrthoDBiEOG63VC1D.
PhylomeDBiP08189.

Family and domain databases

Gene3Di2.60.40.1090. 1 hit.
InterProiIPR008966. Adhesion_dom.
IPR000259. Adhesion_dom_fimbrial.
[Graphical view]
PfamiPF00419. Fimbrial. 1 hit.
[Graphical view]
SUPFAMiSSF49401. SSF49401. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P08189-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRNKPFYLLC AFLWLAVSHA LAADSTITIR GYVRDNGCSV AAESTNFTVD
60 70 80 90 100
LMENAAKQFN NIGATTPVVP FRILLSPCGN AVSAVKVGFT GVADSHNANL
110 120 130 140 150
LALENTVSAA SGLGIQLLNE QQNQIPLNAP SSALSWTTLT PGKPNTLNFY
160 170
ARLMATQVPV TAGHINATAT FTLEYQ
Length:176
Mass (Da):18,715
Last modified:February 1, 1995 - v2
Checksum:i38692EFE6A40121F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti70 – 701P → S in CAA29154 (PubMed:2890081).Curated
Sequence conflicti76 – 761S → L in CAA29154 (PubMed:2890081).Curated
Sequence conflicti81 – 811A → V in CAA29154 (PubMed:2890081).Curated
Sequence conflicti84 – 929AVKVGFTGV → RRKGWVYWR in CAA29154 (PubMed:2890081).Curated
Sequence conflicti107 – 1071V → A in CAA29154 (PubMed:2890081).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05672 Genomic DNA. Translation: CAA29154.1.
U14003 Genomic DNA. Translation: AAA97214.1.
U00096 Genomic DNA. Translation: AAC77274.1.
AP009048 Genomic DNA. Translation: BAE78311.1.
X51655 Genomic DNA. Translation: CAA35969.1.
PIRiS56543.
RefSeqiNP_418738.1. NC_000913.3.
WP_001244827.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77274; AAC77274; b4318.
BAE78311; BAE78311; BAE78311.
GeneIDi948845.
KEGGiecj:JW4281.
eco:b4318.
PATRICi32124232. VBIEscCol129921_4459.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05672 Genomic DNA. Translation: CAA29154.1.
U14003 Genomic DNA. Translation: AAA97214.1.
U00096 Genomic DNA. Translation: AAC77274.1.
AP009048 Genomic DNA. Translation: BAE78311.1.
X51655 Genomic DNA. Translation: CAA35969.1.
PIRiS56543.
RefSeqiNP_418738.1. NC_000913.3.
WP_001244827.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JMRNMR-A23-176[»]
3BFQX-ray1.34F23-37[»]
3BFWX-ray1.80B/D23-37[»]
3BWUX-ray1.76F35-176[»]
3JWNX-ray2.69E/F/K/L23-176[»]
4J3OX-ray3.80F23-176[»]
4XOBX-ray3.00B/D/F/H23-37[»]
ProteinModelPortaliP08189.
SMRiP08189. Positions 23-176.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262749. 3 interactions.
DIPiDIP-9614N.
IntActiP08189. 1 interaction.
MINTiMINT-6491069.
STRINGi511145.b4318.

Proteomic databases

PaxDbiP08189.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77274; AAC77274; b4318.
BAE78311; BAE78311; BAE78311.
GeneIDi948845.
KEGGiecj:JW4281.
eco:b4318.
PATRICi32124232. VBIEscCol129921_4459.

Organism-specific databases

EchoBASEiEB0309.
EcoGeneiEG10313. fimF.

Phylogenomic databases

eggNOGiENOG4108SQA. Bacteria.
ENOG4111HFM. LUCA.
HOGENOMiHOG000260127.
InParanoidiP08189.
KOiK07348.
OMAiYVRDNAC.
OrthoDBiEOG63VC1D.
PhylomeDBiP08189.

Enzyme and pathway databases

BioCyciEcoCyc:EG10313-MONOMER.
ECOL316407:JW4281-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP08189.
PROiP08189.

Family and domain databases

Gene3Di2.60.40.1090. 1 hit.
InterProiIPR008966. Adhesion_dom.
IPR000259. Adhesion_dom_fimbrial.
[Graphical view]
PfamiPF00419. Fimbrial. 1 hit.
[Graphical view]
SUPFAMiSSF49401. SSF49401. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Three fim genes required for the regulation of length and mediation of adhesion of Escherichia coli type 1 fimbriae."
    Klemm P., Christiansen G.
    Mol. Gen. Genet. 208:439-445(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
    Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
    Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "The fimD gene required for cell surface localization of Escherichia coli type 1 fimbriae."
    Klemm P., Christiansen G.
    Mol. Gen. Genet. 220:334-338(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-3.
    Strain: K12.

Entry informationi

Entry nameiFIMF_ECOLI
AccessioniPrimary (citable) accession number: P08189
Secondary accession number(s): Q2M5Z5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: February 1, 1995
Last modified: May 11, 2016
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.